ID W5M609_LEPOC Unreviewed; 622 AA.
AC W5M609;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Zinc finger CCCH-type containing 12A {ECO:0000313|Ensembl:ENSLOCP00000003817.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003817.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003817.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the ZC3H12 family.
CC {ECO:0000256|ARBA:ARBA00010922}.
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DR EMBL; AHAT01009513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01009514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M609; -.
DR STRING; 7918.ENSLOCP00000003817; -.
DR Ensembl; ENSLOCT00000003824.1; ENSLOCP00000003817.1; ENSLOCG00000003232.1.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000155107; -.
DR HOGENOM; CLU_013020_2_1_1; -.
DR InParanoid; W5M609; -.
DR OMA; WSEPYQM; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000003232; Expressed in pharyngeal gill and 10 other cell types or tissues.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0004521; F:RNA endonuclease activity; IBA:GO_Central.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IBA:GO_Central.
DR CDD; cd18729; PIN_Zc3h12-like; 1.
DR Gene3D; 3.40.50.11980; -; 1.
DR InterPro; IPR040546; Rege-1_UBA-like.
DR InterPro; IPR040757; Regnase_1/ZC3H12_C.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12876:SF10; ENDORIBONUCLEASE ZC3H12A; 1.
DR PANTHER; PTHR12876; N4BP1-RELATED; 1.
DR Pfam; PF18561; Regnase_1_C; 1.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
DR Pfam; PF18039; UBA_6; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 305..330
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 305..330
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 69888 MW; 4D8A2F1868D593F1 CRC64;
MLSLNSFPSA TRHSKGSHAI TRMDRGVHYP SREEKQGSPD VAHLEASEFQ MQVDFFRKLG
YSVDEVVAVL HKLGVNADTN TVLGELVRCG ATASEREGVT GSPTGPVLVS RGGSSARTPS
SLSASPPPPP EEDEEEGGHL KPIVIDGSNV AMSHGNKEVF SCRGIQLAVN YFLERGHSDI
TVFVPSWRKE QPRPDVPITD QHILRDLERK KIVVFTPSRR VGGKRVVCYD DRFIVKLAHE
SDGIIVSNDT YRDLQSERPE WRRFIEERLL MYSFVNDKFM PPDDPLGRHG PSLDNFLRKK
PLVQELKRQH CPYGKKCTYG IKCKFYHPER INQTQRSVAD ELRENAKLSA VRAGTPASSL
KDDKKPALSH KSPHPEHSSV FSLEQDIEQK LTLDRRNSLR KGHVTENVVV LRGMPSGRKP
SKKIPFSQSE WSSHPSATNM DSFVFNSQEH LDSGLGSYES QYSEMSRAMS AGANLQPFNQ
DLSSSQNPNI LGRGQHCFSA YGRPTYPAAV NRYSLPNEYS PGVVHAQEYW SDPFQVAPQS
RSGSLQDHRM PQHITGPVSN DQHQWPQPHG NYDKDREEVR KKLLAIFNPY QVDKVMSIFP
YLLDPQRLAA EILTLKSQGG CF
//
